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Literature summary for 1.2.4.2 extracted from

  • Nemeria, N.S.; Gerfen, G.; Nareddy, P.R.; Yang, L.; Zhang, X.; Szostak, M.; Jordan, F.
    The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species (2018), Free Radic. Biol. Med., 115, 136-145 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
succinylphosphonate
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine Homo sapiens
-
[dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Homo sapiens Q96HY7 and Q02218 Q96HY7 i.e. E1 component of the 2-oxoadipate dehydrogenase complex, Q02218 i.e. E1 component of the 2-oxoglutarate dehydrogenase complex
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoadipate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine + CO2
-
?
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine
-
Homo sapiens [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
-
?

Synonyms

Synonyms Comment Organism
2-oxoglutarate dehydrogenase complex
-
Homo sapiens
DHTKD1
-
Homo sapiens
E1a
-
Homo sapiens
E1o
-
Homo sapiens
OGDH
-
Homo sapiens
OGDHC
-
Homo sapiens
ThDP-dependent 2-oxoglutarate dehydrogenase
-
Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21.3
-
2-oxoglutarate at pH 7.0 and 37°C Homo sapiens

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.38
-
succinylphosphonate at pH 7.0 and 37°C Homo sapiens

General Information

General Information Comment Organism
physiological function the 2-oxoadipate dehydrogenase E1a uses the dihydrolipoyl succinyltransferase (E2o) and the dihydrolipoyl dehydrogenase (E3) components of the tricarboxylic acid cycle 2-oxoglutarate dehydrogenase complex (OGDHc) for its activity. 2-Oxoglutarate and 2-oxoadipate can be oxidized by E1a, E1a displays an approximately 49fold preference in catalytic efficiency for 2-oxoadipate over 2-oxoglutarate. E1a forms the thiamidiphosphate-enamine radical from 2-oxoadipate in the oxidative half reaction, and may produce superoxide and H2O2 from decarboxylation of 2-oxoadipate in the forward physiological direction. Once assembled to complex with the same E2o and E3 components, the E1o and E1a display strikingly different regulation: both succinyl-CoA and glutaryl-CoA significantly reduced the E1o activity, but not the activity of E1a Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
142
-
2-oxoglutarate at pH 7.0 and 37°C Homo sapiens